ID A0A1M5NFX1_9BACI Unreviewed; 336 AA.
AC A0A1M5NFX1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SAMN05421807_102207 {ECO:0000313|EMBL:SHG88408.1};
OS Virgibacillus chiguensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=411959 {ECO:0000313|EMBL:SHG88408.1, ECO:0000313|Proteomes:UP000184079};
RN [1] {ECO:0000313|EMBL:SHG88408.1, ECO:0000313|Proteomes:UP000184079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6496 {ECO:0000313|EMBL:SHG88408.1,
RC ECO:0000313|Proteomes:UP000184079};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; FQXD01000002; SHG88408.1; -; Genomic_DNA.
DR RefSeq; WP_073005300.1; NZ_FQXD01000002.1.
DR AlphaFoldDB; A0A1M5NFX1; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000184079; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; NF041438; SepM_fam_S16; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF48; ENDOPEPTIDASE LA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..185
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 186..335
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 336 AA; 37014 MW; 97CBF42BE29293E2 CRC64;
MKKKYIIHIL LVVVAVYFLA IFQLPYYIYK PGGADALNPI VKVEDGFASE GDMHLVTVSG
AKATPMQFLL AKILPHHDVL PIDEVFPEGI TDDEYMHVQL QMMENSQEAS TVVAYQSADK
DISIDFNGVY VAMVVENMPA EGKLELGDRI IGIDDKKVNQ ADDLLDYIET KQVGDSITVK
FVREEKTMTE SITLEAVKDL DNKPGIGIQL VTDRAVSVDP EVKFSSGQIG GPSAGLMFAL
EIYDQLTEED ITHGYEIAGT GEIDYDGNVY RIGGIDKKVV AADREGVDVF FAPNEQGKEG
SNYQIALEKA KEIETDMEIV PVDTFADAIT YLEGLK
//
